Biochemical and structural investigation of the Mrp antiporter, an ancestor of complex I
J. Steiner, Biochemical and Structural Investigation of the Mrp Antiporter, an Ancestor of Complex I, Institute of Science and Technology Austria, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/8353
DOI: 10.15479/AT:ISTA:8353

Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter
J. Steiner, L.A. Sazanov, ELife 9 (2020).
LibreCat: https://research-explorer.ista.ac.at/record/8284
DOI: 10.7554/eLife.59407
WoS: 000562123600001
PMID: 32735215

Molecular mechanisms of mitochondrial redox-coupled proton pumping enzymes
D. Kampjut, Molecular Mechanisms of Mitochondrial Redox-Coupled Proton Pumping Enzymes, Institute of Science and Technology Austria, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/8340
DOI: 10.15479/AT:ISTA:8340

Protective properties of the cultured stem cell proteome studied in an animal model of acetaminophen-induced acute liver failure
A.A. Temnov, K.A. Rogov, A.N. Sklifas, E.V. Klychnikova, M. Hartl, K. Djinovic-Carugo, A. Charnagalov, Molecular Biology Reports (2019).
LibreCat: https://research-explorer.ista.ac.at/record/6352
DOI: 10.1007/s11033-019-04765-z
WoS: 000470332600049

Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase
L. Zhou, L.A. Sazanov, Science 365 (2019).
LibreCat: https://research-explorer.ista.ac.at/record/6859
DOI: 10.1126/science.aaw9144
WoS: 000482464000043
PMID: 31439765

Structural basis of sterol recognition by human hedgehog receptor PTC
C. Qi, G.D. Minin, I. Vercellino, A. Wutz, V.M. Korkhov, Science Advances 5 (2019).
LibreCat: https://research-explorer.ista.ac.at/record/6919
DOI: 10.1126/sciadv.aaw6490
WoS: 000491128800062

Structures of respiratory supercomplex I+II reveal functional and conformational crosstalk
J.A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, L.A. Sazanov, Molecular Cell 75 (2019) 1131–1146.e6.
LibreCat: https://research-explorer.ista.ac.at/record/7395
DOI: 10.1016/j.molcel.2019.07.022
WoS: 000486614200006
PMID: 31492636

Structure and mechanism of mitochondrial proton-translocating transhydrogenase
D. Kampjut, L.A. Sazanov, Nature 573 (2019) 291–295.
LibreCat: https://research-explorer.ista.ac.at/record/6848
DOI: 10.1038/s41586-019-1519-2
WoS: 000485415400061
PMID: 31462775

Mammalian mitochondrial complex I structure and disease causing mutations
K. Fiedorczuk, L.A. Sazanov, Trends in Cell Biology 28 (2018) 835–867.
LibreCat: https://research-explorer.ista.ac.at/record/152
DOI: 10.1016/j.tcb.2018.06.006
WoS: 000445118200007

Structure of respiratory complex I: cMinimald bacterial and cde luxed mammalian versions
L.A. Sazanov, in:, M. Wikström (Ed.), Mechanisms of Primary Energy Transduction in Biology , Royal Society of Chemistry, 2017, pp. 25–59.
LibreCat: https://research-explorer.ista.ac.at/record/444
DOI: 10.1039/9781788010405-00025

Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain
J.A. Letts, L.A. Sazanov, Nature Structural and Molecular Biology 24 (2017) 800–808.
LibreCat: https://research-explorer.ista.ac.at/record/515
DOI: 10.1038/nsmb.3460

Modular architecture and unique teichoic acid recognition features of choline-binding protein L CbpL contributing to pneumococcal pathogenesis
J. Gutierrez-Fernandez, M. Saleh, M. Alcorlo, A. Gómez Mejóa, D. Pantoja Uceda, M. Treviño, F. Vob, M. Abdullah, S. Galán Bartual, J. Seinen, P. Sánchez Murcia, F. Gago, M. Bruix, S. Hammerschmidt, J. Hermoso, Scientific Reports 6 (2016).
LibreCat: https://research-explorer.ista.ac.at/record/1186
DOI: 10.1038/srep38094

Purification of ovine respiratory complex i results in a highly active and stable preparation
J.A. Letts, G. Degliesposti, K. Fiedorczuk, M. Skehel, L.A. Sazanov, Journal of Biological Chemistry 291 (2016) 24657–24675.
LibreCat: https://research-explorer.ista.ac.at/record/1209
DOI: 10.1074/jbc.M116.735142

Atomic structure of the entire mammalian mitochondrial complex i
K. Fiedorczuk, J.A. Letts, G. Degliesposti, K. Kaszuba, M. Skehel, L.A. Sazanov, Nature 538 (2016) 406–410.
LibreCat: https://research-explorer.ista.ac.at/record/1226
DOI: 10.1038/nature19794
PMID: 27595392

The architecture of respiratory supercomplexes
J.A. Letts, K. Fiedorczuk, L.A. Sazanov, Nature 537 (2016) 644–648.
LibreCat: https://research-explorer.ista.ac.at/record/1232
DOI: 10.1038/nature19774

Atomistic determinants of co-enzyme Q reduction at the Qi-site of the cytochrome b complex
P. Postila, K. Kaszuba, P. Kuleta, I. Vattulainen, M. Sarewicz, A. Osyczka, T. Róg, Scientific Reports 6 (2016).
LibreCat: https://research-explorer.ista.ac.at/record/1276
DOI: 10.1038/srep33607

Reversible FMN dissociation from Escherichia coli respiratory complex I
P. Holt, R. Efremov, E. Nakamaru Ogiso, L.A. Sazanov, Biochimica et Biophysica Acta - Bioenergetics 1857 (2016) 1777–1785.
LibreCat: https://research-explorer.ista.ac.at/record/1288
DOI: 10.1016/j.bbabio.2016.08.008

Structure of bacterial respiratory complex I
J. Berrisford, R. Baradaran, L.A. Sazanov, Biochimica et Biophysica Acta - Bioenergetics 1857 (2016) 892–901.
LibreCat: https://research-explorer.ista.ac.at/record/1521
DOI: 10.1016/j.bbabio.2016.01.012

A giant molecular proton pump: structure and mechanism of respiratory complex I
L.A. Sazanov, Nature Reviews Molecular Cell Biology 16 (2015) 375–388.
LibreCat: https://research-explorer.ista.ac.at/record/1638
DOI: 10.1038/nrm3997

Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions
J.A. Letts, L.A. Sazanov, Current Opinion in Structural Biology 33 (2015) 135–145.
LibreCat: https://research-explorer.ista.ac.at/record/1683
DOI: 10.1016/j.sbi.2015.08.008